Search: 135 results found for "Ras-Related C3 Botulinum Toxin Substrate"

Description:

Glycyl-TRNA Synthetase, Mouse Anti Human

Glycine--tRNA ligase, Diadenosine tetraphosphate synthetase, AP-4-A synthetase, Glycyl-tRNA synthetase, GlyRS, GARS, CMT2D, DSMAV, HMN5, SMAD1.

Product # :

ANT-544

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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
GARS is an (alpha)2 dimer which is a member of the class II family of tRNA synthetases. GARS is a glycyl-tRNA synthetase, one of the aminoacyl-tRNA synthetases which charge tRNAs with their cognate amino acids. GARS catalyzes the attachment of glycine to tRNA(Gly). In addition, GARS is able to produce diadenosine tetraphosphate (Ap4A), which is a universal pleiotropic signaling molecule required for cell regulation pathways, by direct condensation of two ATPs. GARS has been demonstrated to be a target of autoantibodies in the human autoimmune diseases, polymyositis or dermatomyositis.
Synonyms
Glycine--tRNA ligase, Diadenosine tetraphosphate synthetase, AP-4-A synthetase, Glycyl-tRNA synthetase, GlyRS, GARS, CMT2D, DSMAV, HMN5, SMAD1.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human GARS mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human GARS amino acids 43-289 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
Clone
PAT4E10AT.
Applications
GARS antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:500.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
GARS antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Cyclin-H, Mouse Anti Human

CCNH, CAK, p34, p37, Cyclin-H, MO15-associated protein.

Product # :

ANT-583

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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
CCNH is part of the cyclin family that is known for its protein abundance through the cell cycle. Cyclins act as regulators of CDK kinases. CCNH forms a complex with CDK7 kinase and ring finger protein MAT1. The kinase complex is able to phosphorylate CDK2 and CDC2 kinases, therefore it functions as a CDK-activating kinase (CAK). CCNH and its kinase collaborator are components of TFIIH, as well as RNA polymerase II protein complexes.
Synonyms
CCNH, CAK, p34, p37, Cyclin-H, MO15-associated protein.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human CCNH mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CCNH amino acids 1-323 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and k light chain.
Clone
PAT3G6AT.
Applications
CCNH antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution for Western blot analysis is 1:1000.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
CCNH antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

RAB, Member RAS Oncogene Family-Like 5 Human Recombinant

Rab-like protein 5 isoform a, Rab-like protein 5, RABL5, RAB, Member RAS Oncogene Family-Like 5.

Product # :

PRO-1472

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Description

RABL5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 208 amino acids (1-185) and having a molecular mass of 23.2 kDa. RABL5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The RABL5 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
RAB, Member RAS Oncogene Family-Like 5 (RABL5) belongs to the Ras superfamily of small GTP-binding proteins. The Ras-related superfamily of guanine nucleotide binding proteins includes the R-Ras, Rap, Ral/Rec and Rho/Rab subfamilies. Rab proteins have an essential role in endocytosis or in biosynthetic protein transport. The transporting process of newly synthesized proteins from the endoplasmic reticulum to various stacks of the Golgi complex and to secretory vesicles includes the movement of carrier vesicles and requires Rab protein function.
Synonyms
Rab-like protein 5 isoform a, Rab-like protein 5, RABL5, RAB, Member RAS Oncogene Family-Like 5.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMLKAKIL FVGPCESGKT VLANFLTESS DITEYSPTQG VRILEFENPH VTSNNKGTGC EFELWDCGGD AKFESCWPAL MKDAHGVVIV FNADIPSHRK EMEMWYSCFV QQPSLQDTQC MLIAHHKPGS GDDKGSLSLS PPLNKLKLVH SNLEDDPEEI RMEFIKYLKS IINSMSESRD REEMSIMT.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Kallikrein-3 Human

Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1

Product # :

ENZ-1172

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Description

Human Kallikrein-3 produced in Human seminal fluid having a molecular mass of approximately 30kD.

Source

Human seminal fluid.

Formulation

The protein solution (0.2 µm filtered) is in 0.09% NaN3, 0.05M phosphate buffer, 150mM NaCl, pH 7.5.

Purity

Greater than 96.0%.

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Introduction
Kallikrein-3 (KLK3) is a part of the kallikrein-related peptidase family. Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins take part in carcinogenesis and some may be prospective cancer and other disease biomarkers. Kallikrein-3 is 1 of the 15 kallikrein subfamily members located in a cluster on chromosome 19 and is a protease present in seminal plasma. KLK3 hydrolyzes semenogelin-1 consequently leading to the liquefaction of the seminal coagulum. KLK3 acts normally in the liquefaction of seminal coagulum, probably by hydrolysis of the high molecular mass seminal vesicle protein. Serum level of the KLK3 protein, called PSA in the clinical setting, is beneficial in the diagnosis and monitoring of prostatic carcinoma.
Synonyms
Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1
Physical Appearance
Sterile Filtered clear solution.
Stability
Human Kallikrein-3 should be stored at 2-8°C. Do not freeze!
Human Virus Test
Starting material donor has been tested and certified negative for antibodies to HIV-1, HIV-2, HCV, HBSAG, Syphilis and HIV/HBV/HCV (PCR).

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

ADP-Ribosylation Factor-Like 3 Human Recombinant

ADP-ribosylation factor-like protein 3, ARL3, ARFL3.

Product # :

PRO-939

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Description

ARL3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (1-182 a.a.) and having a molecular mass of 23kDa.ARL3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ARL3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.1M NaCl, 1mM DTT and 0.1mM PMSF.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
ARL3 (ARFL3) belongs to the ARF-like protein (ARL) subfamily of small GTPases. ARL3 does not activate the cholera toxin ADP-ribosyltranferase contrasting from ARFs. ARL3 is ubiquitously expressed. ARL3 may have a role in maintaining rod photoreceptor cells and regulating microtubule-dependent processes. ARL3 knockdown leads to altered cell morphology, failure of cytokinesis, acetylation of alpha tubulin and an increase in binucleated cells.
Synonyms
ADP-ribosylation factor-like protein 3, ARL3, ARFL3.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMGLLSI LRKLKSAPDQ EVRILLLGLD NAGKTTLLKQ LASEDISHIT PTQGFNIKSV QSQGFKLNVW DIGGQRKIRP YWKNYFENTD ILIYVIDSAD RKRFEETGQE LAELLEEEKL SCVPVLIFAN KQDLLTAAPA SEIAEGLNLH TIRDRVWQIQ SCSALTGEGV QDGMNWVCKN VNAKKK.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Monocyte Chemotactic Protein-1 Rat Recombinant (CCL2)

Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11, Immediate-early serum-responsive JE protein.

Product # :

CHM-315

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Description

Monocyte Chemotactic Protein-1 Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 125 amino acids and having a molecular mass of 14.1 kDa. The MCP-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.

Purity

Greater than 98.0% as determined by SDS-PAGE.

Biological Activity

ED50 =1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg. The biological activity was determined by measuring the dose dependent chemotaxis with human THP-1 cells. The optimal concentration should be determined for each specific application by an initial dose-response assay.

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Introduction
Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belonging to the CC chemokine family that is also known as monocyte chemotactic protein-1 (MCP-1). It is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts and osteoblasts and is under the control of nuclear factor ?B (NF?B). CCL2 recruits immune cells, such as monocytes, to sites of tissue injury and infection. This chemokine is produced as a protein precursor containing signal peptide of 23 amino acids and a mature peptide of 76 amino acids. It is a monomeric polypeptide, with a molecular weightof approximately 13kDa. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans. The cell surface receptors that bind CCL2 are CCR2 and CCR5.
Synonyms
Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11, Immediate-early serum-responsive JE protein.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MCP-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Monocyte Chemotactic Protein-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QPDAVNAPLT CCYSFTGKMI PMSRLENYKR ITSSRCPKEA VVFVTKLKRE ICADPNKEWV QKYIRKLDQN QVRSETTVFY KIASTLRTSA PLNVNLTHKS EANASTLFST TTSSTSVEVT SMTEN.
Background
What is the molecular weight/Mw of CCL2 RAT Protein?
CCL2 RAT Protein has a total Mw of 14.1kDa.

What is the source or expression system of CCL2 RAT Protein?
Escherichia Coli.

What is the Purity of CCL2 RAT Protein?
CCL2 RAT Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL2 RAT Protein?
ED50 =1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg. The biological activity was determined by measuring the dose dependent chemotaxis with human THP-1 cells. The optimal concentration should be determined for each specific application by an initial dose-response assay.

What is the amino acid sequence of CCL2 RAT Protein?
QPDAVNAPLT CCYSFTGKMI PMSRLENYKR ITSSRCPKEA VVFVTKLKRE ICADPNKEWV QKYIRKLDQN QVRSETTVFY KIASTLRTSA PLNVNLTHKS EANASTLFST TTSSTSVEVT SMTEN.

What applications can CCL2 RAT Protein be used in?
CCL2 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL2 RAT Protein?
The endotoxin level is minimal, CCL2 RAT Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL2 RAT that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CCL2 RAT?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Flt3-Ligand Rhesus Macaque Recombinant

Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.

Product # :

CYT-157

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Description

Flt3 Ligand Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 159 amino acids and having a molecular mass of 18.0kDa.The Flt3 Ligand Rhesus Macaque is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The ED50 as calculated by the dose-dependant stimulation of the proliferation of human AML5 cells is less than 1.0ng/ml, corresponding to a specific activity of 1,000,000IU/mg.

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Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
Synonyms
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Flt3 Ligand Rhesus Macaque although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3 Ligand Rhesus Macaque should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Flt3 Ligand in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVPSNLQD EELCGALWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQHP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPRSPGALEA TALTAPQRP
Background
What is the molecular weight/Mw of FLT3-LIGAND RHESUS MACAQUE Protein?
FLT3-LIGAND RHESUS MACAQUE Protein has a total Mw of 18kDa.

What is the source or expression system of FLT3-LIGAND RHESUS MACAQUE Protein?
Escherichia Coli.

What is the Purity of FLT3-LIGAND RHESUS MACAQUE Protein?
FLT3-LIGAND RHESUS MACAQUE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of FLT3-LIGAND RHESUS MACAQUE Protein?
The ED50 as calculated by the dose-dependant stimulation of the proliferation of human AML5 cells is less than 1.0ng/ml, corresponding to a specific activity of 1,000,000IU/mg.

What is the amino acid sequence of FLT3-LIGAND RHESUS MACAQUE Protein?
TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVPSNLQD EELCGALWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQHP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPRSPGALEA TALTAPQRP
What applications can FLT3-LIGAND RHESUS MACAQUE Protein be used in?
FLT3-LIGAND RHESUS MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FLT3-LIGAND RHESUS MACAQUE Protein?
The endotoxin level is minimal, FLT3-LIGAND RHESUS MACAQUE Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interleukin-3 Human Recombinant

MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.

Product # :

CYT-210

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Description

Interleukin-3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 15000 Dalton. The IL-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 0.3 mg/ml of NaHCO3.

Purity

Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000 IU/mg.

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Introduction
IL3 is a potent growth promoting cytokine. This cytokine is capable of supporting the proliferation of a broad range of hematopoietic cell types. It is involved in a variety of cell activities such as cell growth, differentiation and apoptosis. This cytokine has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.
Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Interleukin-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL3 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Interleukin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Met-Thr-Gln.
Background
What is the molecular weight/Mw of IL3 HUMAN Protein?
IL3 HUMAN Protein has a total Mw of 15kDa.

What is the source or expression system of IL3 HUMAN Protein?
Escherichia Coli.

What is the Purity of IL3 HUMAN Protein?
IL3 HUMAN Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of IL3 HUMAN Protein?
The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000 IU/mg.

What is the amino acid sequence of IL3 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Met-Thr-Gln.

What applications can IL3 HUMAN Protein be used in?
IL3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL3 HUMAN Protein?
The endotoxin level is minimal, IL3 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL3 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL3 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.84 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-3 as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Dual Specificity Phosphatase 3, Mouse Anti Human

Dual specificity phosphatase 3, VHR, Vaccinia virus phosphatase VH1-related, Dual specificity protein phosphatase VHR, Vaccinia H1-related phosphatase, serine/threonine specific protein phosphatase, DUSP3.

Product # :

ANT-594

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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
DUSP3 belongs to the dual specificity protein phosphatase subfamily which inactivates their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. DUSP3 negatively regulate members of the mitogen-activated protein kinase superfamily that are related to cellular proliferation and differentiation. DUSP3 is expressed in both breast and ovarian tissues and displays activity both for tyrosine-protein phosphate and serine-protein phosphate, but exhibits a strong preference toward phosphotyrosines, specifically dephosphorylates and inactivates ERK1 and ERK2.
Synonyms
Dual specificity phosphatase 3, VHR, Vaccinia virus phosphatase VH1-related, Dual specificity protein phosphatase VHR, Vaccinia H1-related phosphatase, serine/threonine specific protein phosphatase, DUSP3.
Physical Appearance
Sterile filtered colorless solution.
Immunogen
Anti-human DUSP3 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human DUSP3 amino acids 1-185 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and k light chain.
Clone
PAT9E6AT.
Applications
DUSP3 antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution for Western blot analysis is 1:3000.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
DUSP3 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Flt3 Ligand Mouse Recombinant

Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.

Product # :

CYT-340

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Description

Flt3-Ligand Mouse Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 163 amino acids and having a molecular mass of 18.6kDa. Flt3-Ligand is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The FLT3L Mouse protein was lyophilized from sterile filtered solution containing 10mM sodium phosphate, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, calculated by the dose-dependent proliferation of mouse AML5 cells is 4.96ng/ml, corresponding to a specific activity of 2.0x10⁵ units/mg.

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Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
Synonyms
Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt-3 Ligand should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Flt3l Mouse recombinant in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MTPDCYFSHS PISSNFKVKF RELTDHLLKD YPVTVAVNLQ DEKHCKALWS LFLAQRWIEQ LKTVAGSKMQ TLLEDVNTEI HFVTSCTFQP LPECLRFVQT NISHLLKDTC TQLLALKPCI GKACQNFSRC LEVQCQPDSS TLLPPRSPIA LEATELPEPR PRQ.
Background
What is the molecular weight/Mw of FLT3 LIGAND MOUSE Protein?
FLT3 LIGAND MOUSE Protein has a total Mw of 18.6kDa.

What is the source or expression system of FLT3 LIGAND MOUSE Protein?
Escherichia Coli.

What is the Purity of FLT3 LIGAND MOUSE Protein?
FLT3 LIGAND MOUSE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FLT3 LIGAND MOUSE Protein?
The ED50, calculated by the dose-dependent proliferation of mouse AML5 cells is 4.96ng/ml, corresponding to a specific activity of 2.0x105 units/mg.

What is the amino acid sequence of FLT3 LIGAND MOUSE Protein?
MTPDCYFSHS PISSNFKVKF RELTDHLLKD YPVTVAVNLQ DEKHCKALWS LFLAQRWIEQ LKTVAGSKMQ TLLEDVNTEI HFVTSCTFQP LPECLRFVQT NISHLLKDTC TQLLALKPCI GKACQNFSRC LEVQCQPDSS TLLPPRSPIA LEATELPEPR PRQ.

What applications can FLT3 LIGAND MOUSE Protein be used in?
FLT3 LIGAND MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FLT3 LIGAND MOUSE Protein?
The endotoxin level is minimal, FLT3 LIGAND MOUSE Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Midkine Rat Recombinant

Midkine, MK, Mdk.

Product # :

CYT-747

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Shipped at Room temp

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Description

Midkine Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 120 amino acids and having a molecular mass of 13.2kDa.The Midkine Rat is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration range of 10-100 ng/ml.

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Introduction
Midkine (MK) is the product of a retinoic acid responsive gene, MK, and is a member of a family of heparin binding factors. It contains 121 amino acid residues including 10 conserved cysteine residues, all of which appear to be disulphide linked.
Midkine is expressed during embryogenesis, showing an expression pattern that suggests functions in neurogenesis, cell migration, secondary organogenetic induction, and mesoderm-epithelial interaction.
The widespread downregulation of MK in the adult human is reverted in a number of cancers, in which polypeptides are able to act as both transforming growth factors and promoters of angiogenesis.
Midkine (MK), induces chemotaxis of human neutrophils and was found to trigger mobilization of intracellular calcium of these cells.
Midkine induces histamine release from rat peritoneal mast cells with a rapid response in a dose dependent manner.
Midkine is also a potent stimulator of collagen and glycosaminoglycan synthesis.
Synonyms
Midkine, MK, Mdk.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Midkine Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Midkine Rat should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Midkine Rat in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VAKKKDKVKK GSECSEWTWG PCTPSSKDCG MGFREGTCGA QTQRIHCKVP CNWKKEFGAD CKYKFESWGA CDGSTGTKAR QGTLKKARYN AQCQETIRVT KPCTSKTKSK AKAKKGKGKD.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

RAB5A, Mouse Anti Human

Ras-related protein Rab-5A, RAB5A, RAB5.

Product # :

ANT-337

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Shipped with Ice Packs

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Formulation

1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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Introduction
RAB5A is a member of RAS oncogene family. The small GTPase, RAB5A is a crucial regulatory component of the endocytic pathway. Activation of RAB5A is mediated by GDP-GTP exchange factors (GEFs) that generate the Rab5-GTP complex). RAB5A is required for the fusion of plasma membranes and early endosomes.
Synonyms
Ras-related protein Rab-5A, RAB5A, RAB5.
Immunogen
Anti-human RAB5A mAb is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with recombinant human RAB5A amino acids 1-215 purified from E. coli.
Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
Clone
P3A4AT.
Applications
RAB5A antibody has been tested by ELISA, ICC/IF and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
RAB5A antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Beta Defensin-3 Human Recombinant

HBD3, HBP3, DEFB3, HBD-3, HBP-3, DEFB103.

Product # :

CYT-461

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Description

Beta Defensin-3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 45 amino acids and having a molecular mass of 5161.2 Dalton. The BD-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HBD-3 was lyophilized without additives.

Purity

Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 103A, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense.
Synonyms
HBD3, HBP3, DEFB3, HBD-3, HBP-3, DEFB103.
Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
Stability
Lyophilized Beta Defensin-3 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-3 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Beta Defensin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GIINTLQKYY CRVRGGRCAV LSCLPKEEQI GKCSTRGRKC CRRKK.
Background
Beta Defensin-3 Human Recombinant: Advancements in Antimicrobial Peptide Therapy
Abstract:

Beta Defensin-3 (hBD-3) human recombinant is a promising antimicrobial peptide with broad-spectrum activity against bacteria, viruses, and fungi. This research paper provides an overview of hBD-3, including its properties, mode of action, and potential applications. Additionally, novel methodologies for the production and optimization of hBD-3 human recombinant are discussed, highlighting its future implications in the field of infectious disease management.
Introduction:

The rise of drug-resistant pathogens necessitates exploring alternative therapeutic approaches, such as antimicrobial peptides. Beta Defensin-3 (hBD-3) human recombinant has emerged as a potent candidate due to its broad-spectrum antimicrobial activity. This paper aims to examine the unique features of hBD-3 and propose innovative methodologies for its production and optimization.
Properties and Mode of Action:

hBD-3 possesses a distinct structural composition consisting of 45 amino acids, including an N-terminal loop, three antiparallel β-strands, and a C-terminal α-helix. These structural elements contribute to its ability to disrupt microbial membranes and target selectivity. The mode of action involves electrostatic interactions with negatively charged microbial membranes, leading to membrane disruption and subsequent cell death. Furthermore, hBD-3 exhibits immunomodulatory functions by promoting chemotaxis, enhancing phagocytic activity, and modulating the release of pro-inflammatory cytokines.
Production of hBD-3 Human Recombinant:

Various expression systems, such as bacterial, yeast, and mammalian cell-based platforms, have been explored for the efficient production of hBD-3 human recombinant. Each system offers distinct advantages and challenges, requiring careful selection to achieve high yields and desired protein quality. Optimization strategies, including codon optimization, fusion protein tags, and appropriate growth conditions, have been employed to enhance production efficiency. Purification techniques, such as chromatography and ultrafiltration, have been optimized to isolate high-quality hBD-3 recombinant.
Applications and Future Perspectives:

hBD-3 human recombinant exhibits significant therapeutic potential against drug-resistant pathogens, making it a promising alternative to conventional antibiotics. It also demonstrates promise in wound healing and tissue regeneration by stimulating angiogenesis, extracellular matrix production, and keratinocyte migration. Moreover, the unique physicochemical properties of hBD-3 open avenues for its utilization in nanomedicine, enabling targeted therapy and improved drug delivery.
Conclusion:

hBD-3 human recombinant represents a potent antimicrobial peptide with broad-spectrum activity against diverse pathogens. The optimization of production methodologies and further exploration of its mechanisms of action will contribute to its clinical utility. With its potential applications in infectious disease management, wound healing, and nanomedicine, hBD-3 human recombinant holds promise as a versatile therapeutic agent.
What is the molecular weight/Mw of BD3 Protein?
BD3 Protein has a total Mw of 5.1kDa.

What is the source or expression system of BD3 Protein?
Escherichia Coli.

What is the Purity of BD3 Protein?
BD3 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BD3 Protein?
The biological functionality of BD3 Protein will be determined in the future.

What is the amino acid sequence of BD3 Protein?
GIINTLQKYY CRVRGGRCAV LSCLPKEEQI GKCSTRGRKC CRRKK.

What applications can BD3 Protein be used in?
BD3 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BD3 Protein?
The endotoxin level is minimal, BD3 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

CDNF Rat Recombinant

Cerebral neurotrophic factor, ARMET-like protein 1, Arginine-rich protein mutated in early stage tumors-like 1, Conserved neurotrophic factor, Cdnf, Armetl1.

Product # :

CYT-730

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Shipped at Room temp

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Description

CDNF Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 163 amino acids and having a molecular mass of 18.8kDa.The CDNF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CDNF protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

CDNF Rat is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-25 µg/mL on a nitrocellulose-coated microplate.

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Introduction
CDNF is a member of the ARMET family and acts as a trophic factor for neurons. CDNF inhibits the 6-hydroxy (6-OHDA)-induced degeneration of neurons. When CDNF controlled after 6-OHDA-lesioning, it reestablishes the function and inhibits the degeneration of neurons in substantia nigra. CDNF is universally expressed in neuronal and non-neuronal tissues. The highest levels in the brain are found in the optic nerve and corpus callosum.
Synonyms
Cerebral neurotrophic factor, ARMET-like protein 1, Arginine-rich protein mutated in early stage tumors-like 1, Conserved neurotrophic factor, Cdnf, Armetl1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CDNF should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized CDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QGLEAGVRSR ADCEVCKEFL NRFYNSLLTR GIDFSVDTIE EELISFCADT KGKENRLCYY LGATKDSATK ILGEVTRPMS VHMPTVKICE KLKKMDSQIC ELKYEKKLDL ESVDLWKMRV AELKQILHSW GEECRACAEK HDYVNLIKEL APKYVETRPQ TEL.
Background
What is the molecular weight/Mw of CDNF Protein?
CDNF Protein has a total Mw of 18.8kDa.

What is the source or expression system of CDNF Protein?
Escherichia Coli.

What is the Purity of CDNF Protein?
CDNF Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CDNF Protein?
CDNF Rat is able to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons when immobilized at 5-25 µg/mL on a nitrocellulose-coated microplate.

What is the amino acid sequence of CDNF Protein?
QGLEAGVRSR ADCEVCKEFL NRFYNSLLTR GIDFSVDTIE EELISFCADT KGKENRLCYY LGATKDSATK ILGEVTRPMS VHMPTVKICE KLKKMDSQIC ELKYEKKLDL ESVDLWKMRV AELKQILHSW GEECRACAEK HDYVNLIKEL APKYVETRPQ TEL.

What applications can CDNF Protein be used in?
CDNF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CDNF Protein?
The endotoxin level is minimal, CDNF Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Tumor Necrosis Factor Receptor Mouse Recombinant

Tumor necrosis factor receptor superfamily member 1A, Tumor necrosis factor receptor 1, TNF-R1, Tumor necrosis factor receptor type I, TNF-RI, TNFR-I, p55, p60, CD120a, Tnfrsf1a, Tnfr-1, Tnfr1, FPF, TNF-R, TNFAR, TNFRI, p55-R, TNFR60, Tnfr-2, TNF-R-I, TNF-R55, TNFRp55, TNF-alphaR1, TNFalpha-R1.

Product # :

CYT-774

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Shipped at Room temp

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Description

TNFR Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 191 amino acids and having a molecular mass of 21.1kDa.The TNFR is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNFR protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by its ability to inhibit the TNF-α mediated cytotoxicity in the L-929 cells is less than 1.0 µg/ml, corresponding to a specific activity of > 1000 IU/mg in the presence of 0.1 ng/mL of rMuTNF-a.

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Introduction
TNFR1 belongs to the TNF-receptor superfamily. TNFR1 is a receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha.
There are 2 types of soluble TNF receptors: sTNFR-I and sTNFR-II, which act to neutralize the biological activities of TNF alpha and TNF beta. The levels of these soluble receptors seem to increase as a result of shedding of the extracellular domains of the membrane bound receptors. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury.
TNFR1 is capable of signaling both cell survival and apoptosis. TNFR1-induced apoptosis requires 2 sequential signaling complexes. TNFR1 is capable of activating NF-kappaB, mediate apoptosis, and function as a regulator of inflammation. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNFR1 contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase. Human TNFR1 has a major region which controls cell surface expression. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women.
Germline mutations of the extracellular domains of TNFR1 are linked to the autosomal dominant periodic fever syndrome. The impaired receptor clearance is believed to be a mechanism of the disease. Familial hibernian fever (FHF) is caused by defects in TNFRSF1A gene.
Synonyms
Tumor necrosis factor receptor superfamily member 1A, Tumor necrosis factor receptor 1, TNF-R1, Tumor necrosis factor receptor type I, TNF-RI, TNFR-I, p55, p60, CD120a, Tnfrsf1a, Tnfr-1, Tnfr1, FPF, TNF-R, TNFAR, TNFRI, p55-R, TNFR60, Tnfr-2, TNF-R-I, TNF-R55, TNFRp55, TNF-alphaR1, TNFalpha-R1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TNFR although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TNFR should be stored at 4C between 2-7 days and for future use below -18C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized TNFR in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
IHPSGVTGLV PSLGDREKRD SLCPQGKYVH SKNNSICCTK CHKGTYLVSD CPSPGRDTVC RECEKGTFTA SQNYLRQCLS CKTCRKEMSQ VEISPCQADK DTVCGCKENQ FQRYLSETHF QCVDCSPCFN GTVTIPCKET QNTVCNCHAG FFLRESECVP CSHCKKNEEC MKLCLPPPLA NVTNPQDSGT A.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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